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Database: UniProt
Entry: A0A0X3S2A9_9ACTN
LinkDB: A0A0X3S2A9_9ACTN
Original site: A0A0X3S2A9_9ACTN 
ID   A0A0X3S2A9_9ACTN        Unreviewed;       432 AA.
AC   A0A0X3S2A9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   22-NOV-2017, entry version 9.
DE   RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467};
DE            EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467};
GN   Name=apeB {ECO:0000256|HAMAP-Rule:MF_00467};
GN   ORFNames=ADL25_26695 {ECO:0000313|EMBL:KUJ37884.1};
OS   Streptomyces sp. NRRL F-5122.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1609098 {ECO:0000313|EMBL:KUJ37884.1, ECO:0000313|Proteomes:UP000054048};
RN   [1] {ECO:0000313|EMBL:KUJ37884.1, ECO:0000313|Proteomes:UP000054048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-5122 {ECO:0000313|EMBL:KUJ37884.1,
RC   ECO:0000313|Proteomes:UP000054048};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KUJ37884.1}.
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DR   EMBL; LMWH01000241; KUJ37884.1; -; Genomic_DNA.
DR   RefSeq; WP_059130384.1; NZ_LMWH01000241.1.
DR   EnsemblBacteria; KUJ37884; KUJ37884; ADL25_26695.
DR   Proteomes; UP000054048; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:KUJ37884.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054048};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054048};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        86     86       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       157    157       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       408    408       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   432 AA;  46182 MW;  A05C39D8AE6FD563 CRC64;
     MSTSLRFDRG HTDDLMSFLA ASPSPYHAVA HAAERLEKAG FRQVAETDAW DGTSGGRYVL
     RGGAIIAWYV PEGAEAHTPF RIMGAHTDSP NLRVKPRPDS GAHGWRQIAV EIYGGPLLNS
     WLDRDLGLSG RLSLRDGTTR LVNVDRPLLR VPQLAIHLDR SVSAEGLKLD KQRHLQPVWG
     LGDDVRDGDL IAFLEEEFGL ATGEVTGWDL MTHSVEPPAY LGRDKDLVAG PRMDNLLSVH
     AATAALAAVA TSDAGLSYIP VLAAFDHEEN GSQSDTGADG PLLGSVLERS VFARGGSYED
     RARAFAGSIC LSSDTGHAVH PNYAERHDPT HHPRANGGPI LKVNVNNRYA TDGSGRAVFA
     AACEKANVPF QSFVSNNSMP CGTTIGPITA ARHGIRTVDI GAAILSMHST RELCGADDPH
     MLANALVAFL EG
//
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